Enteropathogenic E-coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
Enteropathogenic E-coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
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DOI：
10.1016/s0092-8674(00)80437-7
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发表时间：
1997-11-14
期刊：
影响因子：
64.5
通讯作者：
Finlay, BB
中科院分区：
文献类型：
--
作者：
Kenny, B;DeVinney, R;Finlay, BB
肠致病性E.大肠杆菌（EPEC）属于一类细菌病原体，其诱导上皮细胞肌动蛋白重排，导致粘附细菌下方的基座形成。这需要分泌信号转导和紧密粘附所需的特异性毒力蛋白。EPEC相互作用诱导宿主膜中蛋白质Hp 90的酪氨酸磷酸化，Hp 90是EPEC外膜蛋白质内膜素的受体。hp 90-intimin相互作用是亲密附着和基座形成所必需的。在这里，我们证明了Hp 90实际上是一种细菌蛋白（Tir）。因此，这种细菌病原体将其自身的受体插入哺乳动物细胞表面，然后粘附到哺乳动物细胞表面以触发额外的宿主信号传导事件和肌动蛋白成核。在转移到宿主细胞中时也被酪氨酸磷酸化。
Enteropathogenic E. coli (EPEC) belongs to a group of bacterial pathogens that induce epithelial cell actin rearrangements resulting in pedestal formation beneath adherent bacteria. This requires the secretion of specific virulence proteins needed for signal transduction and intimate adherence. EPEC interaction induces tyrosine phosphorylation of a protein in the host membrane, Hp90, which is the receptor for the EPEC outer membrane protein, intimin. Hp90-intimin interaction is essential for intimate attachment and pedestal formation. Here, we demonstrate that Hp90 is actually a bacterial protein (Tir). Thus, this bacterial pathogen inserts its own receptor into mammalian cell surfaces, to which it then adheres to trigger additional host signaling events and actin nucleation. It is also tyrosine-phosphorylated upon transfer into the host cell.